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Information on EC 1.8.4.14 - L-methionine (R)-S-oxide reductase and Organism(s) Escherichia coli and UniProt Accession P76270

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IUBMB Comments
Requires NADPH. Unlike EC 1.8.4.12, peptide-methionine (R)-S-oxide reductase, this enzyme cannot use peptide-bound methionine (R)-S-oxide as a substrate . Differs from EC 1.8.4.13, L-methionine (S)-S-oxide in that L-methionine (S)-S-oxide is not a substrate.
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This record set is specific for:
Escherichia coli
UNIPROT: P76270
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
tafrmsr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methionine sulfoxide reductase
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine (R)-S-oxide-forming]
Requires NADPH. Unlike EC 1.8.4.12, peptide-methionine (R)-S-oxide reductase, this enzyme cannot use peptide-bound methionine (R)-S-oxide as a substrate [1]. Differs from EC 1.8.4.13, L-methionine (S)-S-oxide in that L-methionine (S)-S-oxide is not a substrate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
fRMsr exhibits the highest Met-(R)-O reductase activity when all components of the NADPHTrxR-Trx system are present in the reaction. The enzyme is not able to reduce L-methionine (S)-S-oxide, Met sulfone, dimethyl sulfoxide, or MetO when present in the synthetic peptide NH2-Pro-Thr-Ser-Met-(RS)-O-Glu-His-Val-NH2. Escherichia coli fRMsr is the first GAF domain family member to show enzymatic activity
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-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine + thioredoxin disulfide + H2O
L-methionine (R)-S-oxide + thioredoxin
show the reaction diagram
-
enzyme specific for free L-methionine-(R)-sulfoxide and not met-R-(o) in peptide linkage
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-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
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-
?
additional information
?
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-
no activity with peptide-L-methionine-(R)-S-oxide
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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DTT can replace NADPH, but is much less effective
NADPH
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absolute requirement
thioredoxin
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omission results in a 70% drop in activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.9
L-methionine (R)-S-oxide
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0.0098
thioredoxin
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.9
L-methionine (R)-S-oxide
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
partially purified by (NH4)2SO4 precipitation (30-60% saturation) from MsrA/MsrB double mutants
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weissbach, H.; Resnick, L.; Brot, N.
Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage
Biochim. Biophys. Acta
1703
203-212
2005
Escherichia coli
Manually annotated by BRENDA team
Etienne, F.; Spector, D.; Brot, N.; Weissbach, H.
A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide
Biochem. Biophys. Res. Commun.
300
378-382
2003
Escherichia coli, Escherichia coli MC1061
Manually annotated by BRENDA team
Lin, Z.; Johnson, L.C.; Weissbach, H.; Brot, N.; Lively, M.O.; Lowther, W.T.
Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function
Proc. Natl. Acad. Sci. USA
104
9597-9602
2007
Escherichia coli (P76270)
Manually annotated by BRENDA team